Evidence of an Enzymatic Source of Off Flavors in “Lipoxygenase-Null” Soybeans

• Published in: Journal of the American Oil Chemists' Society 2009-01, Vol.86 (1), p.59-64
• Main Authors: Iassonova, Diliara R, Johnson, Lawrence A, Hammond, Earl G, Beattie, Samuel E
• Format: Article
• Language: English
• Subjects: Agriculture; Beans; Biological and medical sciences; Biomaterials; Biotechnology; Carbon dioxide; Chemistry; Chemistry and Materials Science; Colleges & universities; Crop production; Defense mechanisms; Enzyme; Fat industries; Fatty acids; Flavor; Food industries; Food products; Food Science; Fruit and vegetable industries; Fundamental and applied biological sciences. Psychology; Glycine max; Heat treatment; Industrial Chemistry/Chemical Engineering; isozymes; Legumes; Lipoxygenase; Lipoxygenase inhibitors; Lipoxygenase‐like enzyme; off flavors; Original Paper; Phosphatidylcholine; Polyunsaturated fatty acids; Sales; Soybean oil; Soybeans; Volatile off‐flavor compounds; volatile organic compounds
• ISSN: 0003-021X; 1558-9331
• DOI: 10.1007/s11746-008-1314-y

The utilization of soybean products as food ingredients and foods is often limited by their beany-grassy flavor. Eliminating seed lipoxygenase (LOX) isozymes 1, 2 and 3 reduces the amounts of volatile off-flavor compounds in stored soybeans and soy products significantly, but they are not completely eliminated. The present work presents evidence that lipoxygenase-null (LOX-null) soybeans contain a LOX-like enzyme that is responsible for the off-flavors in LOX-null soybeans. Volatiles production in triple LOX-null soybeans was terminated by heat treatment, which suggests an enzymatic cause to the off-flavors. The source is LOX-like in that the volatile compounds produced are similar to LOX-generated products of polyunsaturated fatty acids. Oxygen was consumed when a LOX-null protein solution was incubated with crude soybean oil suggesting that the enzyme catalyzed oxygen consuming reactions. The generation of flavor compounds was inhibited by the typical LOX inhibitors propyl gallate and nordihydroguaiaretic acid (NDGA). The enzyme appears to be more active with phosphatidylcholine than with other lipid substrates. The cause of the off-flavors in LOX-null beans appears to have enzyme-like characteristics. This is the first report of the initial characterization of this LOX-like enzyme.